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dc.contributor.authorKathuria, Sagar V.
dc.contributor.authorChan, Alexander
dc.contributor.authorGraceffa, Rita
dc.contributor.authorNobrega, Robert P.
dc.contributor.authorMatthews, C. Robert
dc.contributor.authorIrving, Thomas C.
dc.contributor.authorPerot, Blair
dc.contributor.authorBilsel, Osman
dc.date2022-08-11T08:08:55.000
dc.date.accessioned2022-08-23T16:12:01Z
dc.date.available2022-08-23T16:12:01Z
dc.date.issued2013-08-28
dc.date.submitted2013-09-04
dc.identifier.citationKathuria, S. V., Chan, A., Graceffa, R., Paul Nobrega, R., Robert Matthews, C., Irving, T. C., Perot, B. and Bilsel, O. (2013), Advances in turbulent mixing techniques to study microsecond protein folding reactions. Biopolymers, 99: 888–896. doi: 10.1002/bip.22355. <a href="http://dx.doi.org/10.1002/bip.22355">Link to article on publisher's website</a>
dc.identifier.doi10.1002/bip.22355
dc.identifier.pmid23868289
dc.identifier.urihttp://hdl.handle.net/20.500.14038/33305
dc.description.abstractRecent experimental and computational advances in the protein folding arena have shown that the readout of the one-dimensional sequence information into three-dimensional structure begins within the first few microseconds of folding. The initiation of refolding reactions has been achieved by several means, including temperature jumps, flash photolysis, pressure jumps and rapid mixing methods. One of the most commonly used means of initiating refolding of chemically-denatured proteins is by turbulent flow mixing with refolding dilution buffer, where greater than 99% mixing efficiency has been achieved within 10's of microseconds. Successful interfacing of turbulent flow mixers with complementary detection methods, including time-resolved Fluorescence Spectroscopy (trFL), Förster Resonance Energy Transfer (FRET), Circular Dichroism (CD), Small-Angle X-ray Scattering (SAXS), Hydrogen Exchange (HX) followed by Mass Spectrometry (MS) and Nuclear Magnetic Resonance Spectroscopy (NMR), Infrared Spectroscopy (IR), and Fourier Transform IR Spectroscopy (FTIR), has made this technique very attractive for monitoring various aspects of structure formation during folding. Although continuous-flow (CF) mixing devices interfaced with trFL detection have a dead time of only 30 µs, burst-phases have been detected in this time scale during folding of peptides and of large proteins (e.g., CheY and TIM barrels). Furthermore, a major limitation of CF mixing technique has been the requirement of large quantities of sample. In this brief communication, we will discuss the recent flurry of activity in micromachining and microfluidics, guided by computational simulations, that are likely to lead to dramatic improvements in time resolution and sample consumption for CF mixers over the next few years.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=23868289&dopt=Abstract">Link to article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1002/bip.22355
dc.subjectTurbulent mixing
dc.subjectContinuous flow
dc.subjectProtein folding
dc.subjectApplied Mechanics
dc.subjectBiochemistry
dc.subjectBiophysics
dc.titleAdvances in turbulent mixing techniques to study microsecond protein folding reactions
dc.typeJournal Article
dc.source.journaltitleBiopolymers
dc.source.volume99
dc.source.issue11
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=2853&amp;context=gsbs_sp&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/1834
dc.identifier.contextkey4548317
refterms.dateFOA2022-08-23T16:12:01Z
html.description.abstract<p>Recent experimental and computational advances in the protein folding arena have shown that the readout of the one-dimensional sequence information into three-dimensional structure begins within the first few microseconds of folding. The initiation of refolding reactions has been achieved by several means, including temperature jumps, flash photolysis, pressure jumps and rapid mixing methods. One of the most commonly used means of initiating refolding of chemically-denatured proteins is by turbulent flow mixing with refolding dilution buffer, where greater than 99% mixing efficiency has been achieved within 10's of microseconds. Successful interfacing of turbulent flow mixers with complementary detection methods, including time-resolved Fluorescence Spectroscopy (trFL), Förster Resonance Energy Transfer (FRET), Circular Dichroism (CD), Small-Angle X-ray Scattering (SAXS), Hydrogen Exchange (HX) followed by Mass Spectrometry (MS) and Nuclear Magnetic Resonance Spectroscopy (NMR), Infrared Spectroscopy (IR), and Fourier Transform IR Spectroscopy (FTIR), has made this technique very attractive for monitoring various aspects of structure formation during folding. Although continuous-flow (CF) mixing devices interfaced with trFL detection have a dead time of only 30 µs, burst-phases have been detected in this time scale during folding of peptides and of large proteins (e.g., CheY and TIM barrels). Furthermore, a major limitation of CF mixing technique has been the requirement of large quantities of sample. In this brief communication, we will discuss the recent flurry of activity in micromachining and microfluidics, guided by computational simulations, that are likely to lead to dramatic improvements in time resolution and sample consumption for CF mixers over the next few years.</p>
dc.identifier.submissionpathgsbs_sp/1834
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.source.pages888–896
dc.contributor.studentR. Paul Nobrega


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